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Genome-wide characterization of TAZ binding sites in mammary epithelial cells in temporary and special manner (RNA-seq)

ABSTRACT: Genome-wide characterization of TAZ binding sites in mammary epithelial cells in temporary and special manner (RNA-seq)

PROVIDER: PRJNA1003036 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR25553805_1.fastq.gz	Fastqsanger.gz
	SRR25553805_2.fastq.gz	Fastqsanger.gz
	SRR25553806_1.fastq.gz	Fastqsanger.gz
	SRR25553806_2.fastq.gz	Fastqsanger.gz
	SRR25553807_1.fastq.gz	Fastqsanger.gz

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Genome-wide characterization of TAZ binding sites in mammary epithelial cells in temporary and special manner (ATAC-seq)

Project description:Genome-wide characterization of TAZ binding sites in mammary epithelial cells in temporary and special manner (ATAC-seq)

| PRJNA1003018 | ENA

Genome-wide characterization of TAZ binding sites in mammary epithelial cells in temporary and special manner (ChIP-seq)

Project description:Genome-wide characterization of TAZ binding sites in mammary epithelial cells in temporary and special manner (ChIP-seq)

| PRJNA1003033 | ENA

Genome-wide characterization of TAZ binding sites in mammary epithelial cells in temporary and special manner (ATAC-seq)

Project description:TAZ, one of the key components of Hippo signaling pathway, is a transcription coactivator and plays an important role in cell proliferation, anti-apoptosis, therapeutic resistance, cancer stemness and tumorigenesis. TAZ mediated transcription program through transcription factors, such as TEAD family members. Genome-wide TAZ occupancy is poorly defined. Here, using a tet-inducible TAZ activation in mammary epithelial MCF10A cells, we characterized genome-wide binding sites in different TAZ activation time points. We found vast majority of TAZ binds to distal enhancer and intergenic regions of genes in the early TAZ activation time point and shift to promoter regions in the later TAZ activation time point. We identified three distinctive TAZ binding patterns to its targets. Furthermore, we found TAZ activation results in chromatin architecture alterations. Our studies provide insight of TAZ regulated transcription program in mammary epithelial cells and indicate potential therapeutic targets for breast cancer.

2023-10-16 | GSE240237 | GEO

Genome-wide characterization of TAZ binding sites in mammary epithelial cells in temporary and special manner (RNA-seq)

2023-10-16 | GSE240244 | GEO

Genome-wide characterization of TAZ binding sites in mammary epithelial cells in temporary and special manner (ChIP-seq)

2023-10-16 | GSE240241 | GEO

Temporary Name

Project description:Temporary Short Descriptive Study Title

| PRJEB55127 | ENA

Effect of activated TAZ expression on mammary epithelial cells

Project description:TAZ is a transcriptional effector of hippo pathway. Expression of activated form of TAZ (4SA TAZ) results in significant alteration of gene expression as measured by RNA sequencing. In addition to the already established targets, our analysis identified several unique proteins, which are differentially regulated upon expression of activated TAZ.

2023-11-08 | GSE115057 | GEO

Yap and Taz regulate retinal pigment epithelial cell fate

Project description:The optic vesicle comprises a pool of bi-potential progenitor cells from which the retinal pigment epithelium (RPE) and neural retina fates segregate during ocular morphogenesis. Several transcription factors and signaling pathways have been shown to be important for RPE maintenance and differentiation, but an understanding of the initial fate specification and determination of this ocular cell type is lacking. We show that Yap/Taz-Tead activity is necessary and sufficient for optic vesicle progenitors to adopt RPE identity in zebrafish. A Teadresponsive transgene is expressed within the domain of the optic cup from which RPE arises, and Yap immunoreactivity localizes to the nuclei of prospective RPE cells. yap (yap1) mutants lack a subset of RPE cells and/or exhibit coloboma. Loss of RPE in yap mutants is exacerbated in combination with taz (wwtr1) mutant alleles such that, when Yap and Taz are both absent, optic vesicle progenitor cells completely lose their ability to form RPE. The mechanism of Yap dependent RPE cell type determination is reliant on both nuclear localization of Yap and interaction with a Tead co-factor. In contrast to loss of Yap and Taz, overexpression of either protein within optic vesicle progenitors leads to ectopic pigmentation in a dosagedependent manner. Overall, this study identifies Yap and Taz as key early regulators of RPE genesis and provides a mechanistic framework for understanding the congenital ocular defects of Sveinsson’s chorioretinal atrophy and congenital retinal coloboma. 60 pooled eyes from 36 hpf wild type or vsx2:Gal4/dsRed:14xUAS:YapS87A embryos were pooled for one sample. Three wild type and three vsx2:Gal4/dsRed:14xUAS:YapS87A pools were analyzed for RNA.

2015-08-06 | E-GEOD-71681 | biostudies-arrayexpress

ChIP-seq for TAZ (WWTR1) binding region in C2C12 myoblasts

Project description:We demonstrated that TAZ positively regulates Irs1 gene transcription in muscle. Therefore we designed ChIP-seq experiment to reveal detailed mechanism of regulation. To capture TAZ in chromatin preparation, we made Flag-tagged TAZ expressing and control vector transduced C2C12 cells by retroviral infection. We used FLAG-conjugated beads to capture TAZ-chromatin complexes and ChIP-seq was perforemd. Among many TAZ binding sites, we focused Irs1 regulatory region because our primary purpose was to identify TAZ binding site for the regulation of Irs1 transcription.

2018-12-13 | E-MTAB-6764 | biostudies-arrayexpress

A chaperone-like function of FUS ensures TAZ condensates dynamics and transcriptional activation

Project description:The Hippo pathway plays important roles in organ development, tissue homeostasis, and tumor growth, and its downstream effector TAZ is a transcriptional coactivator that promotes target gene expression through the formation of biomolecular condensates. However, the mechanisms that regulate the biophysical properties of TAZ condensates to enable Hippo signaling are not well understood. Here, using chemical cross-linking combined with an unbiased proteomic approach, we show that FUS associates with TAZ condensates and exerts a chaperone-like effect to maintain their proper liquidity and robust- transcriptional activity. Mechanistically, the low complexity sequence domain of FUS targets the coiled-coil domain of TAZ in a phosphorylation-regulated manner, which ensures the liquidity and dynamicity of TAZ condensates. In cells lacking FUS, TAZ condensates transition into gel/solid-like assembles with immobilized TAZ, leading to reduced expression of target genes and inhibition of pro-tumorigenic activity. Thus, our findings identify a chaperone-like function of FUS in Hippo regulation and demonstrate that appropriate biophysical properties of transcriptional condensates are essential for gene activation.

2023-02-17 | PXD040257 |

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